메뉴 건너뛰기




Volumn 587, Issue 6, 2013, Pages 575-582

Molecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of function

Author keywords

Neurodegenerative disease; Oxidation; Protein misfolding; RNA recognition motif; RRM1; TDP 43

Indexed keywords

BINDING PROTEIN; CYSTEINE; NUCLEIC ACID; RNA RECOGNITION MOTIF 1 PROTEIN; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84875228800     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.01.038     Document Type: Article
Times cited : (59)

References (26)
  • 1
    • 17144426507 scopus 로고    scopus 로고
    • Human, Drosophila, and C. elegans TDP43: Nucleic acid binding properties and splicing regulatory function
    • Y.M. Ayala, S. Pantano, A. D'Ambrogio, E. Buratti, A. Brindisi, and C. Marchetti Human, Drosophila, and C. elegans TDP43: nucleic acid binding properties and splicing regulatory function J. Mol. Biol. 348 2005 575 588
    • (2005) J. Mol. Biol. , vol.348 , pp. 575-588
    • Ayala, Y.M.1    Pantano, S.2    D'Ambrogio, A.3    Buratti, E.4    Brindisi, A.5    Marchetti, C.6
  • 2
    • 0029066110 scopus 로고
    • Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs
    • S.H. Ou, F. Wu, D. Harrich, L.F. García-Martínez, and R.B. Gaynor Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs J. Virol. 69 1995 3584 3596
    • (1995) J. Virol. , vol.69 , pp. 3584-3596
    • Ou, S.H.1    Wu, F.2    Harrich, D.3    García-Martínez, L.F.4    Gaynor, R.B.5
  • 3
    • 2442676753 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: A functional link with disease penetrance
    • E. Buratti, A. Brindisi, F. Pagani, and F.E. Baralle Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: a functional link with disease penetrance Am. J. Hum. Genet. 74 2004 1322 1325
    • (2004) Am. J. Hum. Genet. , vol.74 , pp. 1322-1325
    • Buratti, E.1    Brindisi, A.2    Pagani, F.3    Baralle, F.E.4
  • 4
    • 57649174592 scopus 로고    scopus 로고
    • TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing
    • J.K. Bose, I.-F. Wang, L. Hung, W.-Y. Tarn, and C.-K.J. Shen TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing J. Biol. Chem. 283 2008 28852 28859
    • (2008) J. Biol. Chem. , vol.283 , pp. 28852-28859
    • Bose, J.K.1    Wang, I.-F.2    Hung, L.3    Tarn, W.-Y.4    Shen, C.-K.J.5
  • 5
    • 73949134014 scopus 로고    scopus 로고
    • Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability: Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS)
    • K. Volkening, C. Leystra-Lantz, W. Yang, H. Jaffee, and M.J. Strong Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability: Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS) Brain Res. 1305 2009 168 182
    • (2009) Brain Res. , vol.1305 , pp. 168-182
    • Volkening, K.1    Leystra-Lantz, C.2    Yang, W.3    Jaffee, H.4    Strong, M.J.5
  • 6
    • 79953185674 scopus 로고    scopus 로고
    • Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
    • Polymenidou, M., Lagier-Tourenne, C., Hutt, K.R., Huelga, S.C., Moran, J., Liang, T.Y. et al. (2011) Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43. Nat. Neurosci. 14, 459-468.
    • (2011) Nat. Neurosci. , vol.14 , pp. 459-468
    • Polymenidou, M.1    Lagier-Tourenne, C.2    Hutt, K.R.3    Huelga, S.C.4    Moran, J.5    Et Al., Y.L.T.6
  • 7
    • 79953180492 scopus 로고    scopus 로고
    • Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
    • J.R. Tollervey, T. Curk, B. Rogelj, M. Briese, M. Cereda, and M. Kayikci Characterizing the RNA targets and position-dependent splicing regulation by TDP-43 Nat. Neurosci. 14 2011 452 458
    • (2011) Nat. Neurosci. , vol.14 , pp. 452-458
    • Tollervey, J.R.1    Curk, T.2    Rogelj, B.3    Briese, M.4    Cereda, M.5    Kayikci, M.6
  • 8
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • M. Neumann, D.M. Sampathu, L.K. Kwong, A.C. Truax, M.C. Micsenyi, and T.T. Chou Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis Science 314 2006 130 133
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3    Truax, A.C.4    Micsenyi, M.C.5    Chou, T.T.6
  • 11
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • E. Buratti, and F.E. Baralle Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9 J. Biol. Chem. 276 2001 36337 36343
    • (2001) J. Biol. Chem. , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 12
    • 64549100193 scopus 로고    scopus 로고
    • Structural insights into TDP-43 in nucleic-acid binding and domain interactions
    • P. Kuo, L. Doudeva, Y. Wang, C. Shen, and H. Yuan Structural insights into TDP-43 in nucleic-acid binding and domain interactions Nucleic Acids Res. 37 2009 1799 1808
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1799-1808
    • Kuo, P.1    Doudeva, L.2    Wang, Y.3    Shen, C.4    Yuan, H.5
  • 13
    • 77950377360 scopus 로고    scopus 로고
    • Induction of amyloid fibrils by the C-terminal fragments of TDP-43 in amyotrophic lateral sclerosis
    • A.K.-H. Chen, R.Y.-Y. Lin, E.Z.-J. Hsieh, P.-H. Tu, R.P.-Y. Chen, and T.-Y. Liao Induction of amyloid fibrils by the C-terminal fragments of TDP-43 in amyotrophic lateral sclerosis J. Am. Chem. Soc. 132 2010 1186 1187
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1186-1187
    • Chen, A.K.-H.1    Lin, R.Y.-Y.2    Hsieh, E.Z.-J.3    Tu, P.-H.4    Chen, R.P.-Y.5    Liao, T.-Y.6
  • 14
    • 27844514227 scopus 로고    scopus 로고
    • TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: An important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
    • E. Buratti, A. Brindisi, M. Giombi, S. Tisminetzky, Y.M. Ayala, and F.E. Baralle TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing J. Biol. Chem. 280 2005 37572 37584
    • (2005) J. Biol. Chem. , vol.280 , pp. 37572-37584
    • Buratti, E.1    Brindisi, A.2    Giombi, M.3    Tisminetzky, S.4    Ayala, Y.M.5    Baralle, F.E.6
  • 16
    • 84857997227 scopus 로고    scopus 로고
    • Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking
    • T.J. Cohen, A.W. Hwang, T. Unger, J.Q. Trojanowski, and V.M. Lee Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking EMBO J. 31 2011 1241 1252
    • (2011) EMBO J. , vol.31 , pp. 1241-1252
    • Cohen, T.J.1    Hwang, A.W.2    Unger, T.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 17
    • 60049100937 scopus 로고    scopus 로고
    • Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: Implications for ribonucleocapsid protein packaging
    • C.-K. Chang, Y.-L. Hsu, Y.-H. Chang, F.-A. Chao, M.-C. Wu, and Y.-S. Huang Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging J. Virol. 83 2009 2255 2264
    • (2009) J. Virol. , vol.83 , pp. 2255-2264
    • Chang, C.-K.1    Hsu, Y.-L.2    Chang, Y.-H.3    Chao, F.-A.4    Wu, M.-C.5    Huang, Y.-S.6
  • 18
    • 26844453741 scopus 로고    scopus 로고
    • The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure
    • C.-K. Chang, S.-C. Sue, T.-H. Yu, C.-M. Hsieh, C.-K. Tsai, and Y.-C. Chiang The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure FEBS Lett. 579 2005 5663 5668
    • (2005) FEBS Lett. , vol.579 , pp. 5663-5668
    • Chang, C.-K.1    Sue, S.-C.2    Yu, T.-H.3    Hsieh, C.-M.4    Tsai, C.-K.5    Chiang, Y.-C.6
  • 19
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: Development of a software pipeline
    • W.F. Vranken, W. Boucher, T.J. Stevesn, R.H. Fogh, A. Pajon, and M. Llinas The CCPN data model for NMR spectroscopy: development of a software pipeline Proteins 59 2005 687 696
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1    Boucher, W.2    Stevesn, T.J.3    Fogh, R.H.4    Pajon, A.5    Llinas, M.6
  • 21
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • U.B. Ericsson, B.M. Hallberg, G.T. Detitta, N. Dekker, and P. Nordlund Thermofluor-based high-throughput stability optimization of proteins for structural studies Anal. Biochem. 357 2006 289 298
    • (2006) Anal. Biochem. , vol.357 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    Detitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 24
    • 0032881445 scopus 로고    scopus 로고
    • Strong hydrophobic nature of cysteine residues in proteins
    • N. Nagano, M. Ota, and K. Nishikawa Strong hydrophobic nature of cysteine residues in proteins FEBS Lett. 458 1999 69 71
    • (1999) FEBS Lett. , vol.458 , pp. 69-71
    • Nagano, N.1    Ota, M.2    Nishikawa, K.3
  • 26
    • 63749096466 scopus 로고    scopus 로고
    • High frequency of TARDBP gene mutations in Italian patients with amyotrophic lateral sclerosis
    • L. Corrado, A. Ratti, C. Gellera, E. Buratti, B. Castellotti, and Y. Carlomagno High frequency of TARDBP gene mutations in Italian patients with amyotrophic lateral sclerosis Hum Mutat 30 2009 688 694
    • (2009) Hum Mutat , vol.30 , pp. 688-694
    • Corrado, L.1    Ratti, A.2    Gellera, C.3    Buratti, E.4    Castellotti, B.5    Carlomagno, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.